MMSA_ANOGA
ID MMSA_ANOGA Reviewed; 521 AA.
AC Q7QC84;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Probable methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial;
DE Short=MMSDH;
DE Short=Malonate-semialdehyde dehydrogenase [acylating];
DE EC=1.2.1.18;
DE EC=1.2.1.27;
DE Flags: Precursor;
GN ORFNames=AGAP002499;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
CC -!- FUNCTION: Plays a role in valine and pyrimidine metabolism. Binds fatty
CC acyl-CoA (By similarity). {ECO:0000250|UniProtKB:Q02252}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methyl-3-oxopropanoate + CoA + H2O + NAD(+) = H(+) +
CC hydrogencarbonate + NADH + propanoyl-CoA; Xref=Rhea:RHEA:20804,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57700, ChEBI:CHEBI:57945; EC=1.2.1.27;
CC Evidence={ECO:0000250|UniProtKB:P42412};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxopropanoate + CoA + NAD(+) = acetyl-CoA + CO2 + NADH;
CC Xref=Rhea:RHEA:22992, ChEBI:CHEBI:16526, ChEBI:CHEBI:33190,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.18;
CC Evidence={ECO:0000250|UniProtKB:Q02252};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxopropanoate + CoA + NADP(+) = acetyl-CoA + CO2 + NADPH;
CC Xref=Rhea:RHEA:22988, ChEBI:CHEBI:16526, ChEBI:CHEBI:33190,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.18;
CC Evidence={ECO:0000250|UniProtKB:Q02252};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q02252}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q02252}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000255}.
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DR EMBL; AAAB01008859; EAA07972.4; -; Genomic_DNA.
DR RefSeq; XP_312441.4; XM_312441.5.
DR AlphaFoldDB; Q7QC84; -.
DR SMR; Q7QC84; -.
DR STRING; 7165.AGAP002499-PA; -.
DR PaxDb; Q7QC84; -.
DR GeneID; 1273463; -.
DR KEGG; aga:AgaP_AGAP002499; -.
DR CTD; 1273463; -.
DR VEuPathDB; VectorBase:AGAP002499; -.
DR eggNOG; KOG2449; Eukaryota.
DR HOGENOM; CLU_005391_1_10_1; -.
DR InParanoid; Q7QC84; -.
DR OMA; HGKRAQC; -.
DR OrthoDB; 608999at2759; -.
DR PhylomeDB; Q7QC84; -.
DR Proteomes; UP000007062; Chromosome 2R.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; IBA:GO_Central.
DR GO; GO:0102662; F:malonate-semialdehyde dehydrogenase (acetylating, NAD+) activity; IEA:RHEA.
DR GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating) activity; IBA:GO_Central.
DR GO; GO:0006210; P:thymine catabolic process; IBA:GO_Central.
DR GO; GO:0006574; P:valine catabolic process; IBA:GO_Central.
DR CDD; cd07085; ALDH_F6_MMSDH; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR010061; MeMal-semiAld_DH.
DR PANTHER; PTHR43866; PTHR43866; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01722; MMSDH; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 3: Inferred from homology;
KW Mitochondrion; NAD; Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..521
FT /note="Probable methylmalonate-semialdehyde dehydrogenase
FT [acylating], mitochondrial"
FT /id="PRO_0000043372"
FT ACT_SITE 304
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q02252,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 196..200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 248..253
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 404
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 521 AA; 56714 MW; C32B9871C0464F42 CRC64;
MALLRLVATE CRNVLQRGYS TASVPTTKMF IDGKFVESKT NDWIDLHDPA TNEVVTRVPK
CTQDEMQTAV ESSKKAYKTW RQSSILSRQQ VMLKLQHIIR NNMSELAKNI TKEQGKTLID
AEGDVLRGLQ VVEHCCSITS LQMGETVPNI AKDMDTYSYH LPLGVTAGIA PFNFPAMIPL
WMFPVAITCG NTSIIKPSER VPGATMLLME MLNEAGCPPG VVNVIHGAHD AVNFVCDNPD
IRAVSFVGSD QAGKYIYERA GRNGKRVQCN MGAKNHGVIM ADANKENTLN QLAGAAFGAA
GQRCMALSTA VFVGEARNWI PDLVERARKL KVNAGHLPGT DLGPVISPQS KQRINELVES
GAKEGAKIVL DGRNIKVEGF EKGNFVGPTI ISDVTPNMKC YTEEIFGPVL VCLSVDTIDE
AIELINNNPY GNGTAIFTTN GATARKFVND IDVGQVGVNV PIPVPLPMFS FTGSRGSFLG
DCHFYGKQGI KFYTQTKTVT QLWREGDVSH TKAAVAMPTM K
